Thiol modification of diacylglycerol kinase: dependence upon site membrane disposition and reagent hydrophobicity

FEBS Letters

Czerski, Lech¹  Sanders, Charles R¹ 

[1] Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44107-4970, USA

关键词: Cysteine modification;    Thiol;    Membrane protein;    Diacylglycerol kinase;    Structure;   

DOI  :  10.1016/S0014-5793(00)01457-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Reaction rates were determined between disulfide reagents of varying hydrophobicity and single-cysteine mutants of diacylglycerol kinase, an integral membrane protein. Polar reagents reacted most rapidly with surface-exposed sites. However, a very non-polar reagent also reacted more rapidly with exposed cysteines than with membrane sites. Moreover, this non-polar reagent usually reacted more slowly with membrane sites than did more polar reagents. These results are consistent with the notion that disulfide exchange reactions involving buried cysteines of diacylglycerol kinase are very slow in the membrane interior, such that the competing rates of reactions which occur when normally buried cysteine sites make motional excursions to hydrated regions of the interface can be significant.

【 授权许可】

Unknown